ID   TOX9_COCH4              Reviewed;         278 AA.
AC   N4WQZ8; D2SZX8;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Probable esterase TOX9 {ECO:0000305};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q5BEJ8};
DE   AltName: Full=T-toxin biosynthesis protein TOX9 {ECO:0000303|PubMed:20192833};
GN   Name=TOX9 {ECO:0000303|PubMed:20192833}; ORFNames=COCC4DRAFT_155492;
OS   Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=20192833; DOI=10.1094/mpmi-23-4-0458;
RA   Inderbitzin P., Asvarak T., Turgeon B.G.;
RT   "Six new genes required for production of T-toxin, a polyketide determinant
RT   of high virulence of Cochliobolus heterostrophus to maize.";
RL   Mol. Plant Microbe Interact. 23:458-472(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
RN   [4]
RP   FUNCTION.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=8953776; DOI=10.2307/3870419;
RA   Yang G., Rose M.S., Turgeon B.G., Yoder O.C.;
RT   "A polyketide synthase is required for fungal virulence and production of
RT   the polyketide T-toxin.";
RL   Plant Cell 8:2139-2150(1996).
RN   [5]
RP   FUNCTION.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=12236595; DOI=10.1094/mpmi.2002.15.9.883;
RA   Rose M.S., Yun S.-H., Asvarak T., Lu S.-W., Yoder O.C., Turgeon B.G.;
RT   "A decarboxylase encoded at the Cochliobolus heterostrophus translocation-
RT   associated Tox1B locus is required for polyketide (T-toxin) biosynthesis
RT   and high virulence on T-cytoplasm maize.";
RL   Mol. Plant Microbe Interact. 15:883-893(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=16529376; DOI=10.1094/mpmi-19-0139;
RA   Baker S.E., Kroken S., Inderbitzin P., Asvarak T., Li B.Y., Shi L.,
RA   Yoder O.C., Turgeon B.G.;
RT   "Two polyketide synthase-encoding genes are required for biosynthesis of
RT   the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus.";
RL   Mol. Plant Microbe Interact. 19:139-149(2006).
CC   -!- FUNCTION: Probable esterase; part of the Tox1A locus, one of the 2 loci
CC       that mediate the biosynthesis of T-toxin, a family of linear
CC       polyketides 37 to 45 carbons in length, of which the major component is
CC       41 carbons, and which leads to high virulence to maize (PubMed:8953776,
CC       PubMed:20192833). One of the PKSs (PKS1 or PKS2) could synthesize a
CC       precursor, used subsequently by the other PKS as starter unit, to add
CC       additional carbons (PubMed:16529376). Variability in the length of the
CC       final carbon backbone C35-47 could be achieved by varying the number of
CC       condensation cycles, or use of different starter or extender units or
CC       might be due to decarboxylation of the penultimate product, catalyzed
CC       by DEC1 (PubMed:12236595). Additional proteins are required for the
CC       biosynthesis of T-toxin, including oxidoreductases RED1, RED2, RED3,
CC       LAM1 and OXI1, as well as esterase TOX9 (PubMed:20192833).
CC       {ECO:0000269|PubMed:12236595, ECO:0000269|PubMed:16529376,
CC       ECO:0000269|PubMed:20192833, ECO:0000269|PubMed:8953776}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192833}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the loss of T-Toxin production,
CC       resulting in low virulence for maize (PubMed:20192833).
CC       {ECO:0000269|PubMed:20192833}.
CC   -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR   EMBL; FJ943499; ADB23431.1; -; Genomic_DNA.
DR   EMBL; KB733545; ENH98547.1; -; Genomic_DNA.
DR   RefSeq; XP_014072457.1; XM_014216982.1.
DR   AlphaFoldDB; N4WQZ8; -.
DR   SMR; N4WQZ8; -.
DR   PRIDE; N4WQZ8; -.
DR   EnsemblFungi; ENH98547; ENH98547; COCC4DRAFT_155492.
DR   GeneID; 25839392; -.
DR   HOGENOM; CLU_051938_0_2_1; -.
DR   OrthoDB; 1190789at2759; -.
DR   PHI-base; PHI:2838; -.
DR   Proteomes; UP000012338; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005645; FSH_dom.
DR   Pfam; PF03959; FSH1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..278
FT                   /note="Probable esterase TOX9"
FT                   /id="PRO_0000437646"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        250
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
SQ   SEQUENCE   278 AA;  31373 MW;  2E0F68F0EDE7578F CRC64;
     MVYNPTATFH KKTLTRMKTG LGSNGDILFI QTRALRDQLS SSFRFVYSNG PFFSDPGPGV
     LPVYKDAGPF RSWLRRPLQN RAQEPRLHME AIRKCLEGTM KEDEQSGASG QWVGLMGFSQ
     GARLAASVLF ESQRRQNIQE KGGIVRGYEG DNIETKLWDQ RWQFAVLFSG PAPLIAFCPE
     NDHLSSQSTA EHDPMYRALD NVNCSGELHI TKPTLHVIGV KDEWAPSQRE LYEKYCSKES
     STLVEWEGAH RIPIESSIVK DLCARILVMS KQADFVES